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Gestalt-binding of tropomyosin to actin filaments [PDF]
We argue that the overall behavior of tropomyosin on F−actin cannot be easily discerned by examining thin filaments reduced to their smallest interacting units.
William Lehman
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On the polymerization of tropomyosin
Archives of Biochemistry and Biophysics, 1962Abstract The polymerization of tropomyosin was studied by light scattering, covering a wide range of protein and salt concentrations. Depolymerization of tropomyosin molecules with dilution was found at very dilute protein concentration, a phenomenon which had not been observed.
T, OOI, K, MIHASHI, H, KOBAYASHI
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Journal of Muscle Research and Cell Motility, 2014
Tropomyosin is a two chained α-helical coiled coil protein that binds actin filaments and interacts with various actin binding proteins. Tropomyosin function depends on its ability to move to distinct locations on the surface of actin in response to the binding of different thin filament effectors.
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Tropomyosin is a two chained α-helical coiled coil protein that binds actin filaments and interacts with various actin binding proteins. Tropomyosin function depends on its ability to move to distinct locations on the surface of actin in response to the binding of different thin filament effectors.
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Cold Adaptation of Tropomyosin
Biochemistry, 2011The conformational stability of unphosphorylated and phosphorylated α,α-striated tropomyosins from rabbit and shark (95% identical sequences) has been investigated. Three additional core positions are occupied by atypical amino acids in the protein from shark: Thr179(d), Ser190(a), and Ser211(a).
Michael, Hayley +2 more
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Proceedings of the Royal Society of London. Series B - Biological Sciences, 1953
Abstract In all muscles so far examined there is present an unusual protein to which no function has yet been assigned. It occurs side by side with actin and myosin in the myofibril, and because of its similarity to myosin was named tropomyosin (Bailey 1948).
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Abstract In all muscles so far examined there is present an unusual protein to which no function has yet been assigned. It occurs side by side with actin and myosin in the myofibril, and because of its similarity to myosin was named tropomyosin (Bailey 1948).
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Tryptic Digestion of Tropomyosin A, Tropomyosin B and Myosin
Nature, 1966Two types of tropomyosins co-exist in lamellibranch adductors and in cephalopod muscle1: TMA and TMB, TMA being the protein referred to as invertebrate tropomyosin, or water-insoluble tropomyosin, by Bailey, and TMB the water-soluble variety.
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Structure of Molluscan Tropomyosin
Nature, 1957CERTAIN molluscan smooth muscles contain protein filaments with a regular and characteristic fine structure1–3 to which the name paramyosin has been given4. Neither the chemical nature nor the function of these filaments is understood, and attention is once more drawn to these problems by the recent discovery in the same muscles of an asymmetric ...
J, HANSON +5 more
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Calponin and tropomyosin interactions
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992The interaction between chicken gizzard calponin and tropomyosin was examined using viscosity, light scattering, electron microscopy and affinity chromatography. At neutral pH, 10 mM NaCl and in the absence of Mg2+, calponin induced tropomyosin filaments to form paracrystals thus decreasing the viscosity while increasing dramatically the light ...
T J, Childs +4 more
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2008
Tropomyosins consist of nearly 100% alpha-helix and assemble into paralleldimeric coiled-coils. Nonmusde as well as muscle tropomyosins can form homodimers, however, expression of both muscle alpha and beta tropomyosin subunits results in the preferential formation of stable alpha/beta heterodimers in native muscle.
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Tropomyosins consist of nearly 100% alpha-helix and assemble into paralleldimeric coiled-coils. Nonmusde as well as muscle tropomyosins can form homodimers, however, expression of both muscle alpha and beta tropomyosin subunits results in the preferential formation of stable alpha/beta heterodimers in native muscle.
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Vertebrate and Invertebrate Tropomyosins
Nature, 1957AS a first step toward generalizing the relationship between tropomyosin, actin and myosin found for rabbit skeletal muscle1, we have prepared and examined tropomyosins from the different types of mammalian muscle (cardiac, uterine and smooth), from lower classes within the vertebrate phylum (amphibian, fish and cyclostome) and from representatives of ...
D R, KOMINZ, K, LAKI, F, SAAD
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